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Conserved domains on  [gi|75812976|ref|NP_001028746|]
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archaemetzincin-2 isoform 2 [Homo sapiens]

Protein Classification

archaemetzincin( domain architecture ID 10183538)

archaemetzincin is an M54 family zinc-dependent aminopeptidase, similar to human archaemetzincin-1 that exhibits aminopeptidase activity against neurogranin in vitro

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-239 9.24e-59

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


:

Pssm-ID: 213029  Cd Length: 173  Bit Score: 185.96  E-value: 9.24e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976  95 GDILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysif 174
Cdd:cd11375  54 DDILDALLKLKPPDADCVLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------- 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75812976 175 dnyyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:cd11375 113 -----PPDEGLFLERLLKEAVHELGHLFGLDHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-239 9.24e-59

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 185.96  E-value: 9.24e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976  95 GDILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysif 174
Cdd:cd11375  54 DDILDALLKLKPPDADCVLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------- 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75812976 175 dnyyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:cd11375 113 -----PPDEGLFLERLLKEAVHELGHLFGLDHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
97-239 3.25e-35

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 125.45  E-value: 3.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976  97 ILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsSSDYSIFdn 176
Cdd:COG1913  56 LLDFLSRLKEEDGDKVLGVTDVDLYAPG-LNFVFGLAYLGGRVAVVSTARLRPEFYGL-------------PPDEELF-- 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75812976 177 yyipeitsvlLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:COG1913 120 ----------LERVLKEAVHELGHLFGLGHCPNPRCVMHFSNSLEELDRKPPSFCPSCRRKLR 172
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
97-238 4.94e-23

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 93.07  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   97 ILKFLKKKKPEDAFCVVGITMIDLYpRDSWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysifdn 176
Cdd:NF033823  55 ILDYLLRIRVGGADKVLGVTDVDLY-EPGLNFVFGLAYPGGKVAVVSTARLRNEFYGR---------------------- 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75812976  177 yyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 238
Cdd:NF033823 112 ---EPDEDLFLERLAKEAVHELGHLLGLGHCPNPRCVMHFSNSLDDTDRKSKYFCPSCRRKL 170
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 98-238 1.06e-17

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 78.91  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   98 LKFLKKKKPEDAFCVVGITMIDLYPRdSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktSSSDYSIFDNy 177
Cdd:PRK13267  59 LPLLSRIGRFNGDKNIGITDCDLYYR-GLNFVFGLAYPNLRGAVISTYRLRPEFYG-------------NKPDSELFEE- 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75812976  178 yipeitsvlllRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 238
Cdd:PRK13267 124 -----------RVRKEVTHELGHTLGLEHCDNPRCVMNFSNSVRDVDIKEPNFCGSCQRKL 173
Peptidase_M54 pfam07998
Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been ...
 112-239 4.93e-13

Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been reported to degrade synthetic substrates and peptides.


Pssm-ID: 191923  Cd Length: 176  Bit Score: 65.98  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   112 VVGITMIDLYPrDSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktssSDYSIFdnyyipeitsvlLLRSC 191
Cdd:pfam07998  76 ILPLGSRDQYF-DGYNFVFGIQVSIGNYAVLALSRLIKPFYT---------------EDRELF------------IERVV 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 75812976   192 KTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:pfam07998 128 KEVTHELGHTYGLSHCNNTDCVMNFSNSLKDVDRKAPTFCNNCLRKLK 175
 
Name Accession Description Interval E-value
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 95-239 9.24e-59

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 185.96  E-value: 9.24e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976  95 GDILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysif 174
Cdd:cd11375  54 DDILDALLKLKPPDADCVLGVTDVDLYEPG-LNFVFGLADGGSGVAVVSTARLRPEFYGL-------------------- 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75812976 175 dnyyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:cd11375 113 -----PPDEGLFLERLLKEAVHELGHLFGLDHCPYYACVMNFSNSLEETDRKPPYLCPVCLRKLQ 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
97-239 3.25e-35

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 125.45  E-value: 3.25e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976  97 ILKFLKKKKPEDAFCVVGITMIDLYPRDsWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsSSDYSIFdn 176
Cdd:COG1913  56 LLDFLSRLKEEDGDKVLGVTDVDLYAPG-LNFVFGLAYLGGRVAVVSTARLRPEFYGL-------------PPDEELF-- 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75812976 177 yyipeitsvlLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:COG1913 120 ----------LERVLKEAVHELGHLFGLGHCPNPRCVMHFSNSLEELDRKPPSFCPSCRRKLR 172
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
97-238 4.94e-23

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 93.07  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   97 ILKFLKKKKPEDAFCVVGITMIDLYpRDSWNFVFGQASLTDGVGIFSFARYGSDFYSMhykgkvkklkktsssdysifdn 176
Cdd:NF033823  55 ILDYLLRIRVGGADKVLGVTDVDLY-EPGLNFVFGLAYPGGKVAVVSTARLRNEFYGR---------------------- 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75812976  177 yyiPEITSVLLLRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 238
Cdd:NF033823 112 ---EPDEDLFLERLAKEAVHELGHLLGLGHCPNPRCVMHFSNSLDDTDRKSKYFCPSCRRKL 170
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 98-238 1.06e-17

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 78.91  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   98 LKFLKKKKPEDAFCVVGITMIDLYPRdSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktSSSDYSIFDNy 177
Cdd:PRK13267  59 LPLLSRIGRFNGDKNIGITDCDLYYR-GLNFVFGLAYPNLRGAVISTYRLRPEFYG-------------NKPDSELFEE- 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75812976  178 yipeitsvlllRSCKTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKL 238
Cdd:PRK13267 124 -----------RVRKEVTHELGHTLGLEHCDNPRCVMNFSNSVRDVDIKEPNFCGSCQRKL 173
Peptidase_M54 pfam07998
Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been ...
 112-239 4.93e-13

Peptidase family M54; This is a family of metallopeptidases. Two human proteins have been reported to degrade synthetic substrates and peptides.


Pssm-ID: 191923  Cd Length: 176  Bit Score: 65.98  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75812976   112 VVGITMIDLYPrDSWNFVFGQASLTDGVGIFSFARYGSDFYSmhykgkvkklkktssSDYSIFdnyyipeitsvlLLRSC 191
Cdd:pfam07998  76 ILPLGSRDQYF-DGYNFVFGIQVSIGNYAVLALSRLIKPFYT---------------EDRELF------------IERVV 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 75812976   192 KTLTHEIGHIFGLRHCQWLACLMQGSNHLEEADRRPLNLCPICLHKLQ 239
Cdd:pfam07998 128 KEVTHELGHTYGLSHCNNTDCVMNFSNSLKDVDRKAPTFCNNCLRKLK 175
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 192-206 5.27e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 37.70  E-value: 5.27e-03
                        10
                ....*....|....*
gi 75812976 192 KTLTHEIGHIFGLRH 206
Cdd:cd04275 139 DTATHEVGHWLGLYH 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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